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Space Layout of Low-entropy Hydration Shells Guides Protein Binding by Yang, Lin; Guo, Shuai; Hou, Chengyu; Liao, Chencheng; Li, Jiacheng; Shi, Liping; Ma, Xiaoliang; Jiang, Shenda; Zheng, Bing; Fang, Yi; Ye, Lin; He, Xiaodong is a scholarly article available to read on EtoBox.

What is Space Layout of Low-entropy Hydration Shells Guides Protein Binding about?

Protein-protein binding enables orderly and lawful biological self-organization, and is therefore considered a miracle of nature. Protein-protein binding is steered by electrostatic forces, hydrogen bonding, van der Waals force, and hydrophobic interactions. Among these physical forces, only the hydrophobic interactions can be considered as long-range intermolecular attractions between proteins in intracellular and extracellular fluid. Low-entropy regions of hydration shells around proteins drive hydrophobic attraction among them that essentially coordinate protein-protein docking in rotational-conformational space of mutual orientations at the guidance stage of the binding. Here, an innovative method was developed for identifying the low-entropy regions of hydration shells of given proteins, and we discovered that the largest low-entropy regions of hydration shells on proteins typically cover the binding sites. According to an analysis of determined protein complex structures, shape matching between the largest low-entropy hydration shell region of a protein and that of its partner at the binding sites is revealed as a regular pattern. Protein-protein binding is thus found to be m

Author

Yang, Lin; Guo, Shuai; Hou, Chengyu; Liao, Chencheng; Li, Jiacheng; Shi, Liping; Ma, Xiaoliang; Jiang, Shenda; Zheng, Bing; Fang, Yi; Ye, Lin; He, Xiaodong

Published

2022

Language

EN